Biology:BST1

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Bst1 (Bone marrow stromal cell antigen 1, ADP-ribosyl cyclase 2, CD157) is an enzyme that in humans is encoded by the BST1 gene.[1][2][3] CD157 is a paralog of CD38, both of which are located on chromosome 4 (4p15) in humans.[4]

Bst1 is a stromal cell line-derived glycosylphosphatidylinositol-anchored molecule that facilitates pre-B-cell growth. The deduced amino acid sequence exhibits 33% similarity with CD38. BST1 expression is enhanced in bone marrow stromal cell lines derived from patients with rheumatoid arthritis. The polyclonal B-cell abnormalities in rheumatoid arthritis may be, at least in part, attributed to BST1 overexpression in the stromal cell population.[3]

CD157 and CD38 are both members of the ADP-ribosyl cyclase family of enzymes that catalyze the formation of nicotinamide and adenosine diphosphate ribose (ADPR) or cyclic ADP-ribose (cADPR) from NAD+, although CD157 is a much weaker catalyst than CD38.[5][6][7] cADPR is required for regulation of Ca22+ in cells.[6] Only CD38 hydrolyzed cADPR to ADPR.[7] CD38 is widely expressed in tissues, whereas CD157 is primarily found in gut and lymphoid tissue.[7]

CD157 has an important role in controlling the migration of leukocytes, the adhesion of leukocytes to blood vessel walls, and the passage of leukocytes through blood vessel walls.[4]

CD157 contributes to macrophage killing of the Mycobacterium tuberculosis bacteria responsible for tuberculosis.[8]

CD157 is highly expressed in acute myeloid leukemia, and is being evaluated as a diagnostic sign, as a treatment target, and as a means of monitoring treatment progress.[9]

BST1 and BST2 genes are unregulated by the Nicotinamide (NAM) metabolism pathway.[10]

See also

References

  1. "Human canonical CD157/Bst1 is an alternatively spliced isoform masking a previously unidentified primate-specific exon included in a novel transcript". Scientific Reports 7 (1): 159231. 2017. doi:10.1038/s41598-017-16184-w. PMID 29162908. Bibcode2017NatSR...715923F. 
  2. "BST-1, a surface molecule of bone marrow stromal cell lines that facilitates pre-B-cell growth". Proc Natl Acad Sci U S A 91 (12): 5325–9. Jul 1994. doi:10.1073/pnas.91.12.5325. PMID 8202488. Bibcode1994PNAS...91.5325K. 
  3. 3.0 3.1 "Entrez Gene: BST1 bone marrow stromal cell antigen 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=683. 
  4. 4.0 4.1 "CD38 and CD157: a long journey from activation markers to multifunctional molecules". Cytometry Part B 84 (4): 207–217. 2013. doi:10.1002/cyto.b.21092. PMID 23576305. 
  5. "CD38, CD157, and RAGE as Molecular Determinants for Social Behavior". Cells 9 (1): 62. 2019. doi:10.3390/cells9010062. PMID 31881755. 
  6. 6.0 6.1 "Evolution and function of the ADP ribosyl cyclase/CD38 gene family in physiology and pathology". Physiological Reviews 88 (3): 841–886. 2008. doi:10.1152/physrev.00035.2007. PMID 18626062. 
  7. 7.0 7.1 7.2 "Therapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence". Cell Metabolism 27 (3): 529–547. 2018. doi:10.1016/j.cmet.2018.02.011. PMID 29514064. 
  8. "Roles of CD38 in the Immune Response to Infection". Cells 9 (1): 228. 2020. doi:10.3390/cells9010228. PMID 31963337. 
  9. "CD157: From Myeloid Cell Differentiation Marker to Therapeutic Target in Acute Myeloid Leukemi". Cells 8 (12): 1580. 2019. doi:10.3390/cells8121580. PMID 31817547. 
  10. "Nicotinamide metabolism regulates glioblastoma stem cell maintenance". JCI Insight 2 (10). May 2017. doi:10.1172/jci.insight.90019. PMID 28515364. 

External links

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.